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Nature Structural Biology|August 1, 1997
Trapping and visualization of a covalent enzyme-phosphate intermediateJ E Murphy, B Stec, L Ma, et al.Biochemistry|July 13, 2000
A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: kinetic studies and three-dimensional crystal structuresL Jin, B Stec, E R KantrowitzJournal of Molecular Biology|June 30, 2000
A revised mechanism for the alkaline phosphatase reaction involving three metal ionsB Stec, K M Holtz, E R KantrowitzJournal of Molecular Biology|July 29, 1998
A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structureM K Williams, B Stec, E R KantrowitzThe Journal of Biological Chemistry|March 20, 1999
A model of the transition state in the alkaline phosphatase reactionK M Holtz, B Stec, E R KantrowitzMolecular Microbiology|May 1, 1994
Why are mammalian alkaline phosphatases much more active than bacterial alkaline phosphatases?J E Murphy, E R KantrowitzProtein Science : a Publication of the Protein Society|August 1, 1996
Crystal structures of the active site mutant (Arg-243-->Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coliB Stec, R Abraham, E Giroux, et al.Protein Science : a Publication of the Protein Society|November 1, 1996
Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativityG Lu, B Stec, E L Giroux, et al.Proteins|January 29, 2000
Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 AL Jin, B Stec, W N Lipscomb, et al.Nature Structural Biology|April 27, 2001
Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylaseC P Macol, H Tsuruta, B Stec, et al.Pageof 333